High throughput recombinant protein production of fungal secreted proteins

Andrea Lages Lino Vala, Doris Roth, Morten Nedergaard Grell, Anders Tunlid, Lene Lange

Publikation: Bidrag til tidsskriftKonferenceabstrakt i tidsskriftForskning

Resumé

Secreted proteins are important for both symbiotic and pathogenic interactions between fungi and their hosts. Our research group uses screens and genomic mining to discover novel proteins involved in these processes. To efficiently study the large number of candidate proteins, we are establishing a high-throughput protein production system with a special focus on fungal secreted proteins. We use a ligation independent cloning to clone target genes into expression vectors for E. coli and P. pastoris and a small scale test expression to identify constructs producing soluble protein. Expressed soluble proteins are then produced in larger quantities, purified and assayed for new enzymatic activities. We used transposon-assisted signal sequence trapping (TAST) to identify putative secreted proteins expressed during the interactions between the basidiomycete Paxillus involutus and birch (symbiotic interaction), between fungi of the order Entomophthorales and aphids (pathogenic interaction), and in the mycoparasitic interaction between the oomycetes Pythium oligandrum and P. ultimum. In general, the high-throughput protein production system can lead to a better understanding of fungal/host interactions and can also identify potential industrially useful enzymes.
OriginalsprogEngelsk
TidsskriftFungal Genetics Reports
Vol/bind58 (Suppl)
Sider (fra-til)373
ISSN1941-4757
StatusUdgivet - 2011
BegivenhedThe 26th Fungal Genetics Conference at Asilomar -
Varighed: 15 mar. 201120 mar. 2011

Konference

KonferenceThe 26th Fungal Genetics Conference at Asilomar
Periode15/03/201120/03/2011

Fingerprint

recombinant proteins
proteins
production technology
Pythium oligandrum
Paxillus involutus
Entomophthorales
Pythium ultimum
fungi
Oomycetes
signal peptide
Basidiomycota
Betula
transposons
trapping
Aphidoidea
molecular cloning
clones
Escherichia coli
genomics
gene expression

Citer dette

Vala, A. L. L., Roth, D., Grell, M. N., Tunlid, A., & Lange, L. (2011). High throughput recombinant protein production of fungal secreted proteins. Fungal Genetics Reports, 58 (Suppl), 373.
Vala, Andrea Lages Lino ; Roth, Doris ; Grell, Morten Nedergaard ; Tunlid, Anders ; Lange, Lene. / High throughput recombinant protein production of fungal secreted proteins. I: Fungal Genetics Reports. 2011 ; Bind 58 (Suppl). s. 373.
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Vala, ALL, Roth, D, Grell, MN, Tunlid, A & Lange, L 2011, 'High throughput recombinant protein production of fungal secreted proteins', Fungal Genetics Reports, bind 58 (Suppl), s. 373.

High throughput recombinant protein production of fungal secreted proteins. / Vala, Andrea Lages Lino; Roth, Doris; Grell, Morten Nedergaard; Tunlid, Anders; Lange, Lene.

I: Fungal Genetics Reports, Bind 58 (Suppl), 2011, s. 373.

Publikation: Bidrag til tidsskriftKonferenceabstrakt i tidsskriftForskning

TY - ABST

T1 - High throughput recombinant protein production of fungal secreted proteins

AU - Vala, Andrea Lages Lino

AU - Roth, Doris

AU - Grell, Morten Nedergaard

AU - Tunlid, Anders

AU - Lange, Lene

PY - 2011

Y1 - 2011

N2 - Secreted proteins are important for both symbiotic and pathogenic interactions between fungi and their hosts. Our research group uses screens and genomic mining to discover novel proteins involved in these processes. To efficiently study the large number of candidate proteins, we are establishing a high-throughput protein production system with a special focus on fungal secreted proteins. We use a ligation independent cloning to clone target genes into expression vectors for E. coli and P. pastoris and a small scale test expression to identify constructs producing soluble protein. Expressed soluble proteins are then produced in larger quantities, purified and assayed for new enzymatic activities. We used transposon-assisted signal sequence trapping (TAST) to identify putative secreted proteins expressed during the interactions between the basidiomycete Paxillus involutus and birch (symbiotic interaction), between fungi of the order Entomophthorales and aphids (pathogenic interaction), and in the mycoparasitic interaction between the oomycetes Pythium oligandrum and P. ultimum. In general, the high-throughput protein production system can lead to a better understanding of fungal/host interactions and can also identify potential industrially useful enzymes.

AB - Secreted proteins are important for both symbiotic and pathogenic interactions between fungi and their hosts. Our research group uses screens and genomic mining to discover novel proteins involved in these processes. To efficiently study the large number of candidate proteins, we are establishing a high-throughput protein production system with a special focus on fungal secreted proteins. We use a ligation independent cloning to clone target genes into expression vectors for E. coli and P. pastoris and a small scale test expression to identify constructs producing soluble protein. Expressed soluble proteins are then produced in larger quantities, purified and assayed for new enzymatic activities. We used transposon-assisted signal sequence trapping (TAST) to identify putative secreted proteins expressed during the interactions between the basidiomycete Paxillus involutus and birch (symbiotic interaction), between fungi of the order Entomophthorales and aphids (pathogenic interaction), and in the mycoparasitic interaction between the oomycetes Pythium oligandrum and P. ultimum. In general, the high-throughput protein production system can lead to a better understanding of fungal/host interactions and can also identify potential industrially useful enzymes.

M3 - Conference abstract in journal

VL - 58 (Suppl)

SP - 373

JO - Fungal Genetics Reports

JF - Fungal Genetics Reports

SN - 1941-4757

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Vala ALL, Roth D, Grell MN, Tunlid A, Lange L. High throughput recombinant protein production of fungal secreted proteins. Fungal Genetics Reports. 2011;58 (Suppl):373.